Human Serpin A1/ alpha 1-Antitrypsin Antibody Summary
Accession # P01009
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Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Human Serpin A1/ alpha 1‑Antitrypsin by Western Blot. Western blot shows lysates of human lung tissue, human kidney tissue, HT-29 human colon adenocarcinoma cell line, and Huh-7 human hepatoma cell line. PVDF membrane was probed with 2 µg/mL of Mouse Anti-Human Serpin A1/a1-Antitrypsin Monoclonal Antibody (Catalog # MAB12681) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). Specific bands were detected for Serpin A1/a1-Antitrypsin at approximately 45-60 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Detection of Human Serpin A1/a1‑Antitrypsin by Simple WesternTM. Simple Western lane view shows human plasma, loaded at 0.2 mg/mL. A specific band was detected for Serpin A1/a1‑Antitrypsin at approximately 65 kDa (as indicated) using 20 µg/mL of Mouse Anti-Human Serpin A1/a1‑Antitrypsin Monoclonal Antibody (Catalog # MAB12681). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Serpin A1/alpha 1-Antitrypsin
Serpin A1 is the archetypal member of the Serpin superfamily of the serine protease inhibitors (1). As one of the most abundant proteinase inhibitors in the circulation, it is synthesized in the liver and secreted into the bloodstream with the major function to protect tissues against neutrophil elastase. A severe Serpin A1 deficiency leads to several clinical complications such as pulmonary emphysema, juvenile hepatitis, cirrhosis, and hepatocellular carcinoma (2). The deficiency is caused by point mutations in naturally occurring Serpin A1 variants (over 70 are known). For example, the Z variant (Glu342 to Lys) forms intracellular inclusion bodies, is not secreted, and leads to a severe Serpin A1 deficiency (3).
- Silverman, G.A. et al. (2001) J. Biol. Chem. 276:33293.
- Barbour, K.W. et al. (2002) Genomics 80:515.
- Lomas, D.A. et al. (2002) Biochem. Soc. Trans. 30:89.
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